RIM4_YEAST - dbPTM
RIM4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RIM4_YEAST
UniProt AC P38741
Protein Name Meiotic activator RIM4
Gene Name RIM4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 713
Subcellular Localization
Protein Description Positive regulator of sporulation-specific genes and of sporulation. Required for premeiotic DNA synthesis and meiotic chromosomal segregation. May act in a nutritional signaling pathway..
Protein Sequence MKTEISTADSLRDPPSNGLKADSELVIREDIDQFLPSEVSSLGSDHQNDGEDSDTDSDNFLQDPEDDVDEESTGRGTVTTTSTSTESRGRPSSCIFVASLAAALSDDELCLSVTENFKKYGDLARVKVLRDNANRPYAFVQYNNDHDAKHALIRAQGTLLNGRRLRCEPAKVNRTLYLKNQQSIDFNEISQICEKFGGLEQIVPDRTDNQYTRRYTYPISSANSWFVQFVYRDDAIRAYANLRTDPNWIIEWAQNINVPKNYNLLHKSKFKSSKYHQNNGIINNDGSNNNDNNNSNNNNREDSRRNGDVIEEECGHVHGSDSEEKLTSDGIYDDEDKDSEITIDKRSIFVGQLDKETTREELNRRFSTHGKIQDINLIFKPTNIFAFIKYETEEAAAAALESENHAIFLNKTMHVQYKEVGGRHNRKFSGKNGGSNFNHHQFFSTRSGKTFTGPELNLAPPPINMYRKMSGGSQQESETMMPYMPMGPMPMGPPPPNAASLSDFDMFPPSYSTFMKGMMPLRRKSMPNSWSSPSSKSVNSENESVNGGDENSELPSEIPESSGRYNAANSFTTYNNSSAGNSNNNNNNNNSNSNKSQYKKRYARRSSYGYNEVPPKPYYFQPYYYHPMQYHMGPMGPLHPSQGSAGNHHPYMMVYPMSPPPPSGLDGSMIPPPINVSQSHAANHGSTHVHANEFISNDTGDINEDNKAYSLDY
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
7Phosphorylation-MKTEISTADSLRDP
-CCCCCCCHHHHCCC		39.9027214570
10PhosphorylationTEISTADSLRDPPSN
CCCCCHHHHCCCCCC		23.8827214570
16PhosphorylationDSLRDPPSNGLKADS
HHHCCCCCCCCCCCC		49.2527214570
23PhosphorylationSNGLKADSELVIRED
CCCCCCCCEEEECCH		37.3827214570
82PhosphorylationRGTVTTTSTSTESRG
CCEEEEECCCCCCCC		20.4727214570
84PhosphorylationTVTTTSTSTESRGRP
EEEEECCCCCCCCCC		29.9127214570
87PhosphorylationTTSTSTESRGRPSSC
EECCCCCCCCCCHHH		39.8728889911
158PhosphorylationALIRAQGTLLNGRRL
HHHHHHCCEECCCEE		18.9127214570
183PhosphorylationLYLKNQQSIDFNEIS
EEECCCCCCCHHHHH		17.8627214570
190PhosphorylationSIDFNEISQICEKFG
CCCHHHHHHHHHHHC		13.8127214570
216PhosphorylationNQYTRRYTYPISSAN
CCCEEEEEEECCCCC		22.4727214570
320PhosphorylationECGHVHGSDSEEKLT
HHCCCCCCCCCCCCC		24.0829136822
322PhosphorylationGHVHGSDSEEKLTSD
CCCCCCCCCCCCCCC		49.7229136822
327PhosphorylationSDSEEKLTSDGIYDD
CCCCCCCCCCCCCCC		35.5224961812
328PhosphorylationDSEEKLTSDGIYDDE
CCCCCCCCCCCCCCC		44.2529136822
332PhosphorylationKLTSDGIYDDEDKDS
CCCCCCCCCCCCCCC		23.9124961812
339PhosphorylationYDDEDKDSEITIDKR
CCCCCCCCCEEECCC		36.3227214570
342PhosphorylationEDKDSEITIDKRSIF
CCCCCCEEECCCCEE		21.0424961812
525PhosphorylationMMPLRRKSMPNSWSS
CCCCCCCCCCCCCCC		37.3522369663
529PhosphorylationRRKSMPNSWSSPSSK
CCCCCCCCCCCCCCC		23.5927717283
531PhosphorylationKSMPNSWSSPSSKSV
CCCCCCCCCCCCCCC		31.9919779198
532PhosphorylationSMPNSWSSPSSKSVN
CCCCCCCCCCCCCCC		23.6527214570
535PhosphorylationNSWSSPSSKSVNSEN
CCCCCCCCCCCCCCC		32.1328889911
537PhosphorylationWSSPSSKSVNSENES
CCCCCCCCCCCCCCC		28.6027214570
540PhosphorylationPSSKSVNSENESVNG
CCCCCCCCCCCCCCC		39.3827214570
544PhosphorylationSVNSENESVNGGDEN
CCCCCCCCCCCCCCC		32.2527214570
608PhosphorylationRYARRSSYGYNEVPP
HHHHHHCCCCCCCCC		25.5229734811
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
-KUbiquitinationE3 ubiquitin ligaseRSP5P39940
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RIM4_YEAST !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of RIM4_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IME2_YEASTIME2genetic
10806425
SIC1_YEASTSIC1genetic
11713679
STE50_YEASTSTE50physical
16554755
SLD3_YEASTSLD3physical
16554755
CORO_YEASTCRN1physical
16554755
SSB1_YEASTSSB1physical
19536198
HPC2_YEASTHPC2genetic
27708008
CGR1_YEASTCGR1genetic
27708008
THIK_YEASTPOT1genetic
27708008
SYH1_YEASTSYH1genetic
27708008
HSP73_YEASTSSA3genetic
27708008
TAT1_YEASTTAT1genetic
27708008
SIF2_YEASTSIF2genetic
27708008
RS6A_YEASTRPS6Bgenetic
27708008
RS6B_YEASTRPS6Bgenetic
27708008
YCA2_YEASTYCL002Cgenetic
27708008
RL13A_YEASTRPL13Agenetic
27708008
YD056_YEASTYDR056Cgenetic
27708008
EF2_YEASTEFT2genetic
27708008
DOT1_YEASTDOT1genetic
27708008
YG036_YEASTYGL036Wgenetic
27708008
PALF_YEASTRIM8genetic
27708008
YOR1_YEASTYOR1genetic
27708008
BGL2_YEASTBGL2genetic
27708008
ATG32_YEASTATG32genetic
27708008
MDM35_YEASTMDM35genetic
27708008
DGR2_YEASTDGR2genetic
27708008
DCOR_YEASTSPE1genetic
27708008
DID2_YEASTDID2genetic
27708008
DNM1_YEASTDNM1genetic
27708008
PSR1_YEASTPSR1genetic
27708008
YEH1_YEASTYEH1genetic
27708008
EIF3J_YEASTHCR1genetic
27708008
NGL3_YEASTNGL3genetic
27708008
MAC1_YEASTMAC1genetic
27708008
SHH3_YEASTSHH3genetic
27708008
YM22_YEASTYMR144Wgenetic
27708008
YM24_YEASTYMR147Wgenetic
27708008
ATC8_YEASTDNF3genetic
27708008
INP2_YEASTINP2genetic
27708008
TMA23_YEASTTMA23genetic
27708008
OCA2_YEASTOCA2genetic
27708008
PHO23_YEASTPHO23genetic
27708008
MSB4_YEASTMSB4genetic
27708008
LPX1_YEASTLPX1genetic
27708008
YO385_YEASTYOR385Wgenetic
27708008
CHL1_YEASTCHL1genetic
27708008
COX10_YEASTCOX10genetic
27708008
ATG13_YEASTATG13genetic
27708008
RIM4_YEASTRIM4physical
26411291
H4_YEASTHHF1genetic
29674565
TOR1_YEASTTOR1genetic
29674565
SC61A_YEASTSEC61genetic
29674565
SWC5_YEASTSWC5genetic
29674565
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RIM4_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-525, AND MASSSPECTROMETRY.

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